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LOCUS WP_000781074 428 aa linear BCT 08-JUN-2021 ACCESSION WP_000781074 VERSION WP_000781074.1 KEYWORDS RefSeq. SOURCE Enterobacteriaceae ORGANISM Enterobacteriaceae Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales. REFERENCE 1 (residues 1 to 428) AUTHORS Parsot,C. TITLE Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase JOURNAL EMBO J 5 (11), 3013-3019 (1986) PUBMED 3098560 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: TIGR00260.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..428 /organism="Enterobacteriaceae" /db_xref="taxon:543" gene 1..428 /gene="thrC" Protein 1..428 /product="threonine synthase" /EC_number="4.2.3.1" /GO_function="GO:0004795 - threonine synthase activity [Evidence IEA]" /GO_process="GO:0009088 - threonine biosynthetic process [Evidence IEA]" /calculated_mol_wt=46983 Region 2..423 /region_name="Thr-synth_2" /note="Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria; cd01560" /db_xref="CDD:107203" Site order(107,248..249,376) /site_type="other" /note="pyridoxal 5'-phosphate binding site [chemical binding]" /db_xref="CDD:107203" Site 107 /site_type="active" /note="catalytic residue [active]" /db_xref="CDD:107203" ORIGIN 1 mklynlkdhn eqvsfaqavt qglgknqglf fphdlpefsl teidemlkld fvtrsakils 61 afigdeipqe ileervraaf afpapvanve sdvgclelfh gptlafkdfg grfmaqmlth 121 iagdkpvtil tatsgdtgaa vahafyglpn vkvvilyprg kisplqeklf ctlggnietv 181 aidgdfdacq alvkqafdde elkvalglns ansinisrll aqicyyfeav aqlpqetrnq 241 lvvsvpsgnf gdltagllak slglpvkrfi aatnvndtvp rflhdgqwsp katqatlsna 301 mdvsqpnnwp rveelfrrki wqlkelgyaa vddettqqtm relkelgyts ephaavayra 361 lrdqlnpgey glflgtahpa kfkesveail getldlpkel aeradlplls hnlpadfaal 421 rklmmnhq